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6FWF

Low resolution structure of Neisseria meningitidis qNOR

Replaces:  6ELH
Functional Information from GO Data
ChainGOidnamespacecontents
A0004129molecular_functioncytochrome-c oxidase activity
A0009060biological_processaerobic respiration
A0009486molecular_functioncytochrome bo3 ubiquinol oxidase activity
A0015990biological_processelectron transport coupled proton transport
A0016020cellular_componentmembrane
A0016491molecular_functionoxidoreductase activity
A0020037molecular_functionheme binding
A0022904biological_processrespiratory electron transport chain
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues25
Detailsbinding site for residue HEM A 1001
ChainResidue
ATYR78
AALA608
AGLY612
APHE613
AILE615
AASN616
ALEU621
AGLN625
AGLY626
ASER630
AHIS633
AGLU411
AALA637
ALEU638
ATYR642
AHEM1002
ACA1003
AFE1004
ATYR412
ATRP486
AHIS490
AGLU494
AHIS542
AVAL564
ALEU567

site_idAC2
Number of Residues24
Detailsbinding site for residue HEM A 1002
ChainResidue
AGLY76
ATYR78
AGLN294
AVAL295
AGLY298
AGLY299
ATHR301
AALA302
AARG332
AHIS335
AILE336
AGLU411
ATYR412
AHIS635
ALEU638
APHE639
AMET682
AARG721
AARG724
AASP728
APHE731
AILE732
AHEM1001
ACA1003

site_idAC3
Number of Residues5
Detailsbinding site for residue CA A 1003
ChainResidue
AGLY76
ATYR78
AGLU411
AHEM1001
AHEM1002

site_idAC4
Number of Residues4
Detailsbinding site for residue FE A 1004
ChainResidue
AHIS490
AHIS541
AHIS542
AHEM1001

Functional Information from PROSITE/UniProt
site_idPS00077
Number of Residues57
DetailsCOX1_CUB Heme-copper oxidase catalytic subunit, copper B binding region signature. WWVVHLwVegffevfataafafvfynmgfvrrstatastlaaaaifmlggvpgtlHH
ChainResidueDetails
ATRP486-HIS542

224572

PDB entries from 2024-09-04

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